Give the names of both non-polar amino acids shown in the image Complex I is Comples II is I COO- I H-C-CH3 NH COO- H-C-CH₂-CH NH 11 CH3 CH3
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- Write the following oligopeptide using the one letter code for the amino acids: Cys-His-lle-Leu-Glu N.B. Use upper case characters only, pleaseDraw the structure of this peptide: N-Met-His-Tyr-Leu-Asp-Ser-Arg-Leu-CAfter a polypeptide chain has been synthesized, certain amino acids in the peptide may become modified. For each modified amino acid, identify the standard amino acid from which it is derived. Enter the unabbreviated name of the standard amino acid. OH I *NH,CH,–C–CH,CH,—CH–COO H C *NH₂ standard amino acid: Identify the modification that yields the first amino acid depicted. addition of a hydroxyl group addition of an amino group modification of the existing amino group modification of the existing hydroxyl group elongation of the side chain by the addition of a -CH₂- group
- Amino Acid: Asn-Met-Ser-Ile-Phe-Arg-Cys-Tyr-Lys What is the one letter code of this amino acid and what is its classification? What is the side chain description (e.g. amide, aromatic etc.)Provide the correct three-letter abbreviation for the following amino acid: Gln ← H₂N-CH-C-C 1 CH3 Ala Arg Asn Asp Cys Glu Gly His lle Leu Lys 包Draw a peptide for cys-asn- pro-gly (Using the same format in picture)
- Cut the following protein with the Serine Proteolytic enzyme Trypsin. How many peptide fragments are present after the protein is treated with Trypsin? Val-lle-Arg-Lys-Leu-Arg-Gly-Ala-Lys-lle 6. 10Cut the following protein with the Serine Proteolytic enzyme Trypsin. How many peptide fragments are present after the protein is treated with Trypsin? Ala-Leu-Arg-Gly-Met-Val-Arg-Lys-Ala O 2 6. 8.Identify the polar amino acids, the aromatic amino acids,and the sulfur-containing amino acids, given a peptide with thefollowing amino acid sequence:Val-Met-Ser-Ile-Phe-Arg-Cys-Tyr-Leu
- After the polypeptide shown below was treated with maleic anhydride, it was hydrolyzed by trypsin. (After a polypeptide is treated with maleic anhydride, trypsin will cleave the polypeptide only on the C-side of arginine.) Gly-Ala-Asp-Ala-Leu-Pro-Gly-Ile-Leu-Val-Arg-Asp-Val-Gly-Lys-Val-Glu-Val-Phe-Glu-Ala-Gly-Arg-Ala-Glu-Phe-Lys-Glu-Pro-Arg-Leu-Val-Met-Lys-Val-Glu-Gly-Arg-Pro-Val-Gly-Ala-Gly-Leu-Trp In what order will the fragments be eluted from an anion-exchange column using a buffer of pH = 5?Translate the following amino acid sequence into one-letter code: Glu-Leu-Val-Ile-Ser-IleSer-Leu-IleVal-Ile-Asn-Gly-Ile-Asn-Leu-Ala-SerValGlu-Gly-Ala-SerConsider the following two peptides: I. N-Pro-Pro - Glu - Glu - Tyr - His - Cys - Ala - Glu - Gln - Lys - Leu - Ser - Ser - Phe-Leu- Thr - C II. N-Pro-Pro - Lys - Arg - Gly - Tyr - His - Gly - Glu - Asp - Glu - Asp - Glu - Ser - Gly-Phe- Tyr-C Give three reasons why_peptide I is more likely to form an alpha helix in aqueous solution at pH 7.0. Your reasons may include why_peptide Il is less likely to form an alpha helix